Linked Life Data

2164927

Source:http://linkedlifedata.com/resource/pubmed/id/2164927

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-8-30
pubmed:abstractText
We have previously reported that FSH stimulates flux of 45Ca2+ into cultured Sertoli cells from immature rats via voltage-sensitive and voltage-independent calcium channels. In the present study, we show that this effect of FSH does not require cholera toxin (CT)- or pertussis toxin (PT)-sensitive guanine nucleotide binding (G) protein or activation of adenylate cyclase (AC). Significant stimulation of 45Ca2+ influx was observed within 1 min, and maximal response (3.2-fold over basal levels) was achieved within 2 min after exposure to FSH. FSH-stimulated elevations in cellular cAMP paralleled increases in 45Ca2+ uptake, suggesting a possible coupling of AC activation to 45Ca2+ influx. (Bu)2cAMP, however, was not able to enhance 45Ca2+ uptake over basal levels at a final concentration of 1000 microM, although a concentration-related increase in androstenedione conversion to estradiol was evident. Exposure of Sertoli cells to CT (10 ng/ml) consistently stimulated basal levels of androstenedione conversion to estradiol but had no effect on basal levels of 45Ca2+ uptake. Similarly, CT had no effect on FSH-induced 45Ca2+ uptake, but potentiated FSH-stimulated estradiol synthesis. PT (10 ng/ml) augmented basal and FSH-stimulated estradiol secretion without affecting 45Ca2+ influx. The adenosine analog N6-phenylisopropyladenosine, which binds to Gi-coupled adenosine receptors on Sertoli cells, inhibited FSH-stimulated androgen conversion to estradiol in a dose-related (1-1000 nM) manner, but FSH-stimulated 45Ca2+ influx remained unchanged. Our results show that in contrast to FSH-stimulated estradiol synthesis, the flux of 45Ca2+ into Sertoli cells in response to FSH is not mediated either directly or indirectly by CT- or PT-sensitive G protein, nor does it require activation of AC. Our data further suggest that the FSH receptor itself may function as a calcium channel.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
949-56
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2164927-Adenylate Cyclase, pubmed-meshheading:2164927-Adenylate Cyclase Toxin, pubmed-meshheading:2164927-Animals, pubmed-meshheading:2164927-Biological Transport, Active, pubmed-meshheading:2164927-Bucladesine, pubmed-meshheading:2164927-Calcium, pubmed-meshheading:2164927-Carbon Radioisotopes, pubmed-meshheading:2164927-Cells, Cultured, pubmed-meshheading:2164927-Cholera Toxin, pubmed-meshheading:2164927-Enzyme Activation, pubmed-meshheading:2164927-Follicle Stimulating Hormone, pubmed-meshheading:2164927-GTP-Binding Proteins, pubmed-meshheading:2164927-Kinetics, pubmed-meshheading:2164927-Male, pubmed-meshheading:2164927-Pertussis Toxin, pubmed-meshheading:2164927-Rats, pubmed-meshheading:2164927-Receptors, FSH, pubmed-meshheading:2164927-Sertoli Cells, pubmed-meshheading:2164927-Virulence Factors, Bordetella
pubmed:year
1990
pubmed:articleTitle
Follicle-stimulating hormone receptor-mediated uptake of 45Ca2+ by cultured rat Sertoli cells does not require activation of cholera toxin- or pertussis toxin-sensitive guanine nucleotide binding proteins or adenylate cyclase.
pubmed:affiliation
Department of Biochemistry, Albany Medical College, New York 12208.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.